作者: Jinping Du , Bernd H. A. Rehm
DOI: 10.1007/S10529-017-2473-4
关键词:
摘要: To overcome laborious and costly procedures often associated with therapeutic protein production purification, in vivo polyester immobilized sortase is explored for the of human tumor necrosis factor alpha (TNFα) interferon 2b (IFNα2b) by Escherichia coli. Hybrid genes encoding PhaC-Sortase-TNFα or PhaC-Sortase-IFNα2b fusions (with a LPETG recognition signal immediately before TNFα IFNα2b), mediated intracellular (polyhydroxyalkanoate, PHA) beads Upon isolation respective PHA beads, pure soluble IFNα2b was released activating via addition CaCl2 triglycine. each were recognized corresponding conformational antibodies an ELISA assay. In could be exploited purification high-value proteins without downstream processing.